The accumulation of oxidized isoforms of chicken triosephosphate isomerase during aging and development
Triosephosphate isomerase (TPI) from mammals undergoes two specific deamidations (Asn-15 and Asn-71) which destabilize the isologous dimer and lead to the degradation of the protein. In aging cells and tissues, the deamidated isoforms accumulate apparently due to age-related changes in protein turno...
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Veröffentlicht in: | Mechanisms of ageing and development 1990-11, Vol.56 (2), p.179-186 |
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creator | Noelle Gracy, K. Tang, C.Y. Ümit Yüksel, K. Gracy, Robert W. |
description | Triosephosphate isomerase (TPI) from mammals undergoes two specific deamidations (Asn-15 and Asn-71) which destabilize the isologous dimer and lead to the degradation of the protein. In aging cells and tissues, the deamidated isoforms accumulate apparently due to age-related changes in protein turnover. Chicken TPI lacks one of these sites (
i.e., Asn 71 → Lys), but also exhibits unstable isoforms. These isoforms are the result of the specific oxidations which occur both
in vitro and
in vivo. Electrophoretic analyses of various tissues from chicken show that the most oxidized isoform, which is present in adult tissues, is only present in small quantities in tissues of the newborn chick. Moreover, embryonic tissues contain almost exclusively the fully reduced form of TPI. Thus, it appears that oxidation rather than deamidation constitutes the first step in the degradation of avian TPI. TPI may be the first example of a protein which has evolved two different types of modifications (deamidation and oxidation) which trigger its degradation. The accumulation of both deamidated and oxidized isoforms in different species may provide clues to the underlying basis for the accumulation of modified proteins in aging. |
doi_str_mv | 10.1016/0047-6374(90)90008-4 |
format | Article |
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i.e., Asn 71 → Lys), but also exhibits unstable isoforms. These isoforms are the result of the specific oxidations which occur both
in vitro and
in vivo. Electrophoretic analyses of various tissues from chicken show that the most oxidized isoform, which is present in adult tissues, is only present in small quantities in tissues of the newborn chick. Moreover, embryonic tissues contain almost exclusively the fully reduced form of TPI. Thus, it appears that oxidation rather than deamidation constitutes the first step in the degradation of avian TPI. TPI may be the first example of a protein which has evolved two different types of modifications (deamidation and oxidation) which trigger its degradation. The accumulation of both deamidated and oxidized isoforms in different species may provide clues to the underlying basis for the accumulation of modified proteins in aging.</description><identifier>ISSN: 0047-6374</identifier><identifier>EISSN: 1872-6216</identifier><identifier>DOI: 10.1016/0047-6374(90)90008-4</identifier><identifier>PMID: 2290356</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>Aging ; Aging - metabolism ; Amino Acid Sequence ; Animals ; Chick Embryo ; Chicken ; Chickens ; Development ; Isoenzymes - metabolism ; Isozymes ; Oxidation ; Oxidation-Reduction ; Tissue Distribution ; Triose-Phosphate Isomerase - chemistry ; Triose-Phosphate Isomerase - metabolism ; Triosephosphate isomerase</subject><ispartof>Mechanisms of ageing and development, 1990-11, Vol.56 (2), p.179-186</ispartof><rights>1990</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-fe95abb4a0cc546610b1f6d5665f8a12344f7984c55e714543970755263c260f3</citedby><cites>FETCH-LOGICAL-c357t-fe95abb4a0cc546610b1f6d5665f8a12344f7984c55e714543970755263c260f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0047-6374(90)90008-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2290356$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Noelle Gracy, K.</creatorcontrib><creatorcontrib>Tang, C.Y.</creatorcontrib><creatorcontrib>Ümit Yüksel, K.</creatorcontrib><creatorcontrib>Gracy, Robert W.</creatorcontrib><title>The accumulation of oxidized isoforms of chicken triosephosphate isomerase during aging and development</title><title>Mechanisms of ageing and development</title><addtitle>Mech Ageing Dev</addtitle><description>Triosephosphate isomerase (TPI) from mammals undergoes two specific deamidations (Asn-15 and Asn-71) which destabilize the isologous dimer and lead to the degradation of the protein. In aging cells and tissues, the deamidated isoforms accumulate apparently due to age-related changes in protein turnover. Chicken TPI lacks one of these sites (
i.e., Asn 71 → Lys), but also exhibits unstable isoforms. These isoforms are the result of the specific oxidations which occur both
in vitro and
in vivo. Electrophoretic analyses of various tissues from chicken show that the most oxidized isoform, which is present in adult tissues, is only present in small quantities in tissues of the newborn chick. Moreover, embryonic tissues contain almost exclusively the fully reduced form of TPI. Thus, it appears that oxidation rather than deamidation constitutes the first step in the degradation of avian TPI. TPI may be the first example of a protein which has evolved two different types of modifications (deamidation and oxidation) which trigger its degradation. The accumulation of both deamidated and oxidized isoforms in different species may provide clues to the underlying basis for the accumulation of modified proteins in aging.</description><subject>Aging</subject><subject>Aging - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Chick Embryo</subject><subject>Chicken</subject><subject>Chickens</subject><subject>Development</subject><subject>Isoenzymes - metabolism</subject><subject>Isozymes</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Tissue Distribution</subject><subject>Triose-Phosphate Isomerase - chemistry</subject><subject>Triose-Phosphate Isomerase - metabolism</subject><subject>Triosephosphate isomerase</subject><issn>0047-6374</issn><issn>1872-6216</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAQgIMouj7-gUJPoodqkubRXgQRXyB40XPIJpPdaNvUpF3UX2_rLh69zMDMNzPMh9AxwRcEE3GJMZO5KCQ7q_B5hTEuc7aFZqSUNBeUiG00-0P20H5KbyNDGBW7aJfSChdczNDiZQmZNmZohlr3PrRZcFn49NZ_g818Ci7EJk1Fs_TmHdqsjz4k6JYhdUvdw8Q0EHWCzA7Rt4tML35jazMLK6hD10DbH6Idp-sER5t8gF7vbl9uHvKn5_vHm-un3BRc9rmDiuv5nGlsDGdCEDwnTlguBHelJrRgzMmqZIZzkIRxVlQSS86pKAwV2BUH6HS9t4vhY4DUq8YnA3WtWwhDUiWmkvBCjiBbgyaGlCI41UXf6PilCFaTXzXJU5M8VWH161excexks3-YN2D_hjZCx_7Vug_jkysPUSXjoTVgfQTTKxv8_wd-AO9_ioY</recordid><startdate>19901101</startdate><enddate>19901101</enddate><creator>Noelle Gracy, K.</creator><creator>Tang, C.Y.</creator><creator>Ümit Yüksel, K.</creator><creator>Gracy, Robert W.</creator><general>Elsevier Ireland Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19901101</creationdate><title>The accumulation of oxidized isoforms of chicken triosephosphate isomerase during aging and development</title><author>Noelle Gracy, K. ; Tang, C.Y. ; Ümit Yüksel, K. ; Gracy, Robert W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-fe95abb4a0cc546610b1f6d5665f8a12344f7984c55e714543970755263c260f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Aging</topic><topic>Aging - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Chick Embryo</topic><topic>Chicken</topic><topic>Chickens</topic><topic>Development</topic><topic>Isoenzymes - metabolism</topic><topic>Isozymes</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Tissue Distribution</topic><topic>Triose-Phosphate Isomerase - chemistry</topic><topic>Triose-Phosphate Isomerase - metabolism</topic><topic>Triosephosphate isomerase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Noelle Gracy, K.</creatorcontrib><creatorcontrib>Tang, C.Y.</creatorcontrib><creatorcontrib>Ümit Yüksel, K.</creatorcontrib><creatorcontrib>Gracy, Robert W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Mechanisms of ageing and development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Noelle Gracy, K.</au><au>Tang, C.Y.</au><au>Ümit Yüksel, K.</au><au>Gracy, Robert W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The accumulation of oxidized isoforms of chicken triosephosphate isomerase during aging and development</atitle><jtitle>Mechanisms of ageing and development</jtitle><addtitle>Mech Ageing Dev</addtitle><date>1990-11-01</date><risdate>1990</risdate><volume>56</volume><issue>2</issue><spage>179</spage><epage>186</epage><pages>179-186</pages><issn>0047-6374</issn><eissn>1872-6216</eissn><abstract>Triosephosphate isomerase (TPI) from mammals undergoes two specific deamidations (Asn-15 and Asn-71) which destabilize the isologous dimer and lead to the degradation of the protein. In aging cells and tissues, the deamidated isoforms accumulate apparently due to age-related changes in protein turnover. Chicken TPI lacks one of these sites (
i.e., Asn 71 → Lys), but also exhibits unstable isoforms. These isoforms are the result of the specific oxidations which occur both
in vitro and
in vivo. Electrophoretic analyses of various tissues from chicken show that the most oxidized isoform, which is present in adult tissues, is only present in small quantities in tissues of the newborn chick. Moreover, embryonic tissues contain almost exclusively the fully reduced form of TPI. Thus, it appears that oxidation rather than deamidation constitutes the first step in the degradation of avian TPI. TPI may be the first example of a protein which has evolved two different types of modifications (deamidation and oxidation) which trigger its degradation. The accumulation of both deamidated and oxidized isoforms in different species may provide clues to the underlying basis for the accumulation of modified proteins in aging.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>2290356</pmid><doi>10.1016/0047-6374(90)90008-4</doi><tpages>8</tpages></addata></record> |
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subjects | Aging Aging - metabolism Amino Acid Sequence Animals Chick Embryo Chicken Chickens Development Isoenzymes - metabolism Isozymes Oxidation Oxidation-Reduction Tissue Distribution Triose-Phosphate Isomerase - chemistry Triose-Phosphate Isomerase - metabolism Triosephosphate isomerase |
title | The accumulation of oxidized isoforms of chicken triosephosphate isomerase during aging and development |
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